› 1h7a

X-ray diffraction
2.75Å resolution

Structural basis for allosteric substrate specificity regulation in class III ribonucleotide reductases: NRDD in complex with dATP

Released:
DOI: 10.2210/pdb1h7a/pdb
PDB entry 1h7a coloured by chain, front view.
PDB entry 1h7a coloured by chain, side view.
PDB entry 1h7a coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Structural basis for allosteric substrate specificity regulation in anaerobic ribonucleotide reductases.
Larsson KM, Andersson J, Sjöberg BM, Nordlund P, Logan DT
Structure 9 739-50 (2001)
PMID: 11587648

Function and Biology Details

Reaction catalysed: 
Ribonucleoside 5'-triphosphate + formate = 2'-deoxyribonucleoside 5'-triphosphate + CO(2) + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139363 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Anaerobic ribonucleoside-triphosphate reductase Chain: A
Molecule details ›
Chain: A
Length: 605 amino acids
Theoretical weight: 68.06 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli
UniProt:
  • Canonical: P07071 (Residues: 1-605; Coverage: 100%)
Gene names: 49.1, 55.11/55.13, SUNY, nrdD
Sequence domains: Glycine radical
Structure domains: Anaerobic Ribonucleotide-triphosphate Reductase Large Chain

Ligands and Environments

3 bound ligands:
Ligand DTP 1 x DTP
Ligand FE2 1 x FE2
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P43212
Unit cell:
a: 98.36Å b: 98.36Å c: 244.12Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.215 0.258
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Ribonucleotide reductases.
Nordlund et al. (2006)
7 more

2 mentions without citation

An Iron Reservoir to the Catalytic Metal: THE RUBREDOXIN IRON IN AN EXTRADIOL DIOXYGENASE.
Liu et al. (2015)
1 more